The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.4.19.2     
Accepted name: peptidyl-glycinamidase
Reaction: Cleavage of C-terminal glycinamide from polypeptides
Other name(s): carboxyamidase; peptidyl carboxy-amidase; peptidyl-aminoacylamidase; carboxamidopeptidase; peptidyl amino acid amide hydrolase
Comments: Inactivates vasopressin and oxytocin by splitting off glycinamide. Also cleaves ester substrates of trypsin and chymotrypsin. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. The toad skin enzyme is inhibited by diisopropyl fluorophosphate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-14-0
References:
1.  Fruhaufová, L., Suska-Brezezinska, E., Barth, T. and Rychlik, I. Rat liver enzyme inactivating oxytocin and its deamino-carba analogues. Coll. Czech. Chem. Commun. 38 (1973) 2793–2798.
2.  Nardacci, N.J., Mukhopadhyay, S. and Campbell, B.J. Partial purification and characterization of the antidiuretic hormone in toad bladder. Biochim. Biophys. Acta 377 (1975) 146–157. [PMID: 1122284]
3.  Simmons, W.H. and Walter, R. Carboxamidopeptidase: purificaction and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin. Biochemistry 19 (1980) 39–48. [PMID: 6766314]
[EC 3.4.19.2 created 1978 as EC 3.4.15.2, transferred 1981 to EC 3.4.19.2]
 
 


Data © 2001–2016 IUBMB
Web site © 2005–2016 Andrew McDonald